| Activity |
|---|
| Catalytic type | Serine |
| Peplist | Included in the Peplist with identifier PL00275 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.39
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (23 cleavages) |
| Activity status | human: active (Caughey, 2004)
mouse: active (Springman & Serafin, 1995)
|
| Physiology | Hydrolyses extracellular matrix proteins and others after release from mast cells. Second to peptidyl-dipeptidase A, the major angiotensin II-forming enzyme (Caughey et al., 2000; Muilenburg et al., 2002). Polymorphism rs1800875 in the promoter region of the human CMA1 gene is significantly associated with atopic eczema (Weidinger et al., 2005). |
| Pharmaceutical relevance | Possible drug target in immune-related diseases of lung. Also, there is an indication that an inhibitor can reduce post-operative adhesions (Okamoto et al., 2002). An inhibitor is reported to prevent the development of intimal hyperplasia in balloon-injured arteries (Takai et al., 2003). Results obtained in a dog model have led to the suggestion that chronic inhibition of chymase can prevent cardiac remodelling in heart failure (Matsumoto et al., 2003). The therapeutic potential of chymase inhibitors has been reviewed by Doggrell & Wanstall (2004). Takai et al., 2004 propose that chymase is also a novel target for preventing vascular diseases. |
| Pathways |
KEGG | Renin-angiotensin system |
|
Other databases
| TREEFAM | http://www.treefam.org/family/TF333630 |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/-/-/FY -/eld/-/- (based on 107 cleavages) |
